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Pharmacogenomics: Identification of New Drug Targets

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Related Experiment Video

Updated: Jul 8, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Development and application of Hsp90 inhibitors.

David B Solit1, Gabriela Chiosis

  • 1Department of Medicine and the Human Oncology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, United States.

Drug Discovery Today
|January 15, 2008
PubMed
Summary

Heat shock protein 90 (Hsp90) is a key target for diseases like cancer and neurodegeneration. This review covers Hsp90

Area of Science:

  • Molecular biology
  • Cellular biology
  • Disease mechanisms

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone.
  • Its role in protein folding and stability is vital for cellular function.
  • Dysregulation of Hsp90 is implicated in various pathologies.

Purpose of the Study:

  • To review the multifaceted roles of Hsp90 in disease.
  • To explore Hsp90's involvement in cancer and neurodegenerative disorders.
  • To summarize Hsp90's function in infectious diseases and therapeutic strategies.

Main Methods:

  • Literature review of existing research on Hsp90.
  • Analysis of Hsp90's function in different disease models.
  • Examination of preclinical and clinical data for Hsp90 inhibitors.

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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

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Related Experiment Videos

Last Updated: Jul 8, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
09:39

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

Main Results:

  • Hsp90 is essential for maintaining the transformed phenotype in cancer cells.
  • Hsp90 plays a significant role in the progression of neurodegenerative diseases.
  • Hsp90 is implicated in the life cycle of fungal and viral pathogens.

Conclusions:

  • Hsp90 is a validated therapeutic target across diverse diseases.
  • Targeting Hsp90 offers a promising strategy for cancer, neurodegenerative, and infectious diseases.
  • Further development of Hsp90 inhibitors is warranted for clinical application.